X-ray and NMR structure of human Bcl-xL, an inhibitor of programmed cell death View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

1996-05

AUTHORS

Steven W. Muchmore, Michael Sattler, Heng Liang, Robert P. Meadows, John E. Harlan, Ho Sup Yoon, David Nettesheim, Brian S. Chang, Craig B. Thompson, Sui-Lam Wong, Shi-Chung Ng, Stephen W. Fesik

ABSTRACT

THE Bcl-2 family of proteins regulate programmed cell death by an unknown mechanism1. Here we describe the crystal and solution structures of a Bcl-2 family member, Bcl-xL (ref. 2). The structures consist of two central, primarily hydrophobic α-helices, which are surrounded by amphipathic helices. A 60-residue loop connecting helices αl and α2 was found to be flexible and non-essential for anti-apoptotic activity. The three functionally important Bcl-2 homology regions (BH1, BH2 and BH3)3–5 are in close spatial proximity and form an elongated hydrophobic cleft that may represent the binding site for other Bcl-2 family members. The arrangement of the α-helices in Bcl-xL is reminiscent of the membrane translocation domain of bacterial toxins, in particular diphtheria toxin and the colicins6. The structural similarity may provide a clue to the mechanism of action of the Bcl-2 family of proteins. More... »

PAGES

335-341

Journal

TITLE

Nature

ISSUE

6580

VOLUME

381

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/381335a0

    DOI

    http://dx.doi.org/10.1038/381335a0

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1003038902

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/8692274


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    24 schema:description THE Bcl-2 family of proteins regulate programmed cell death by an unknown mechanism1. Here we describe the crystal and solution structures of a Bcl-2 family member, Bcl-xL (ref. 2). The structures consist of two central, primarily hydrophobic α-helices, which are surrounded by amphipathic helices. A 60-residue loop connecting helices αl and α2 was found to be flexible and non-essential for anti-apoptotic activity. The three functionally important Bcl-2 homology regions (BH1, BH2 and BH3)3–5 are in close spatial proximity and form an elongated hydrophobic cleft that may represent the binding site for other Bcl-2 family members. The arrangement of the α-helices in Bcl-xL is reminiscent of the membrane translocation domain of bacterial toxins, in particular diphtheria toxin and the colicins6. The structural similarity may provide a clue to the mechanism of action of the Bcl-2 family of proteins.
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